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- W2319224384 abstract "Glycosylation is one of the most important protein modifications in biological systems. It plays a critical role in protein folding, trafficking, and stability as well as cellular events such as immune response and cell-to-cell communication. Aberrant protein glycosylation is correlated with several diseases including diabetes, cancer, and infectious diseases. The heterogeneity of glycans makes comprehensive identification of protein glycosylation sites very difficult by MS because it is challenging to match mass spectra to peptides that contain different types of unknown glycans. We combined a chemical deglycosylation method with LC–MS-based proteomics techniques to comprehensively identify protein N-glycosylation sites in yeast. On the basis of the differences in chemical properties between the amide bond of the N-linkage and the glycosidic bond of the O-linkage of sugars, O-linked sugars were removed and only the innermost N-linked GlcNAc remained, which served as a mass tag for MS analysis. This chemical deglycosylation method allowed for the identification of 555 protein N-glycosylation sites in yeast by LC–MS, which is 46% more than those obtained from the parallel experiments using the Endo H cleavage method. A total of 250 glycoproteins were identified, including 184 membrane proteins. This method can be extensively used for other biological samples." @default.
- W2319224384 created "2016-06-24" @default.
- W2319224384 creator A5005446460 @default.
- W2319224384 creator A5010861834 @default.
- W2319224384 creator A5019829909 @default.
- W2319224384 date "2014-02-10" @default.
- W2319224384 modified "2023-09-26" @default.
- W2319224384 title "Comprehensive Analysis of Protein N-Glycosylation Sites by Combining Chemical Deglycosylation with LC–MS" @default.
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- W2319224384 doi "https://doi.org/10.1021/pr401000c" @default.
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